Purification of Uridine Phosphorylase from Crude Extracts of Escherichia Coli Employing High-Speed Countercurrent Chromatography With an Aqueous Two-Phase Solvent System

Y. W. Lee Research Triangle Institute, Chemistry and Life Sciences, P. O. Box 12194, Research Triangle Park, North Carolina, 27709

Y. Shibusawa NIH-NHLBI Bethesda, Maryland, 20892

F. T. Chen Research Triangle Institute, Chemistry and Life Sciences, P. O. Box 12194, Research Triangle Park, North Carolina, 27709

J. Myers North Carolina Central University, Department of Chemistry, Durham, North Carolina, 27707

J. M. Schooler North Carolina Central University, Department of Chemistry, Durham, North Carolina, 27707

Y. Ito NIH-NHLBI Bethesda, Maryland, 20892

Abstract

This is a preliminary report on a novel liquid-liquid parti tioning chromatography method for the purification of recombinant protein, uridine phosphorylase (UrdPase). This system utilizes an aqueous two-phase solvent system, consisting of polyethylene glycol and phosphate buffer, with a newly developed high-speed countercurrent centrifuge (X-axis, XLL type). The system is capable of purifying crude recombinant UrdPase in an efficient manner.

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Purification of Uridine Phosphorylase from Crude Extracts of Escherichia Coli Employing High-Speed Countercurrent Chromatography With an Aqueous Two-Phase Solvent System

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Purification of Uridine Phosphorylase from Crude Extracts of Escherichia Coli Employing High-Speed Countercurrent Chromatography With an Aqueous Two-Phase Solvent System

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